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(Received for publication, September 3, 1996, and in revised form, October 4, 1996)
From the Bruton's tyrosine kinase (Btk), a cytoplasmic
protein-tyrosine kinase, plays a pivotal role in B cell activation and
development. Mutations in the pleckstrin homology (PH) domain of the
Btk gene cause human X-linked agammaglobulinemia (XLA) and
murine X-linked immunodeficiency (Xid). In this paper, we report that
the PH domain of Btk functions as an inositol 1,3,4,5-tetrakisphosphate
(IP4), inositol 1,3,4,5,6-pentakisphosphate, and inositol
1,2,3,4,5,6-hexakisphosphate (IP6) binding domain
(Kd of approximately 40 nM for
IP4), and that all of the XLA (Phe replaced by Ser at
position 25 (F25S), R28H, T33P, V64F, and V113D) and Xid mutations
(R28C) found in the PH domain result in a dramatic reduction of
IP4 binding activity. Furthermore, the rare alternative
splicing variant, with 33 amino acids deleted in the PH domain,
corresponding to exon 3 of the Btk gene, also impaired
IP4 binding capacity. In contrast, a gain-of-function mutant called Btk*, which carries a E41K mutation in the PH domain, binds IP6 with two times higher affinity than the wild
type. Our data suggest that B cell differentiation is closely
correlated with the IP4 binding capacity of the PH domain
of Btk.
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30303-30306
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
§
,§
,§
and§
Molecular Neurobiology Laboratory, Tsukuba
Life Science Center, The Institute of Physical and Chemical Research
(RIKEN), 3-1-1 Koyadai, Tsukuba, Ibaraki 305, Japan,
§ Department of Molecular Neurobiology, Institute of Medical
Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan, and 
Calciosignal Net Project, Exploratory Research for
Advanced Technology (ERATO), 2-9-3 Shimo-meguro, Meguro-ku, Tokyo 153, Japan
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L. E. Rameh, A.-k. Arvidsson, K. L. Carraway III, A. D. Couvillon, G. Rathbun, A. Crompton, B. VanRenterghem, M. P. Czech, K. S. Ravichandran, S. J. Burakoff, et al. A Comparative Analysis of the Phosphoinositide Binding Specificity of Pleckstrin Homology Domains J. Biol. Chem., August 29, 1997; 272(35): 22059 - 22066. [Abstract] [Full Text] [PDF]
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